Manduca sexta gloverin binds microbial components and is active against bacteria and fungi

被引:41
作者
Xu, Xiao-Xia [1 ,2 ]
Zhong, Xue [1 ]
Yi, Hui-Yu [1 ,3 ]
Yu, Xiao-Qiang [1 ]
机构
[1] Univ Missouri, Sch Biol Sci, Div Cell Biol & Biophys, Kansas City, MO 64110 USA
[2] S China Agr Univ, Coll Nat Resources & Environm, Guangzhou 510642, Guangdong, Peoples R China
[3] S China Agr Univ, Coll Anim Sci, Guangzhou 510642, Guangdong, Peoples R China
关键词
Gloverin; Toll-Spatzle pathway; Lipopolysaccharide; Lipoteichoic acid; Peptidoglycan; Antimicrobial activity; ANTIMICROBIAL PEPTIDE GENES; TOBACCO HORNWORM; ANTIBACTERIAL PROTEIN; FUNCTIONAL-ANALYSIS; LIPOTEICHOIC ACID; IMMUNE-RESPONSE; DROSOPHILA; LIPOPOLYSACCHARIDE; EXPRESSION; SILKWORM;
D O I
10.1016/j.dci.2012.06.012
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
Hyalophora gloveri gloverin is a glycine-rich and heat stable antimicrobial protein with activity mainly against Escherichia coli. However. Spodoptera exigua gloverin is active against a Gram-positive bacterium but inactive against E. coli. In this study, we investigated expression profile, binding ability and antimicrobial activity of Manduca sexta gloverin (MsGlv). Msglv transcript was detected in several tissues of naive larvae with higher levels in the midgut and testis. Expression of Msglv mRNA in larvae was up-regulated by active Spatzle-C108 and peptidoglycans (PGs) of E. coli and Staphylococcus aureus, and the activation was blocked by pre-injection of antibody to M. sexta Toll, suggesting that Msglv expression is regulated by the Toll-Spatzle pathway. Recombinant MsGlv bound to the O-specific antigen and outer core carbohydrate of lipopolysaccharide (LPS). Gram-positive lipoteichoic acid (LTA) and PG, and laminarin, but not to E. coli PG or mannan. MsGlv was active against Bacillus cereus, Saccharomyces cerevisiae and Cryptococcus neoformans, but was almost inactive against E. coli and S. aureus. Our results suggest that gloverins are active against some bacteria and fungi. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:275 / 284
页数:10
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